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Volume 271, Number 47, Issue of November 22, 1996 pp. 30227-30232
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Isolation of a Calcium-binding Phosphoprotein from the Oocytes and Hemolymph of the Blood-sucking Insect Rhodnius prolixus

(Received for publication, July 8, 1996, and in revised form, August 26, 1996)

Mário A. C. Silva-Neto , Geórgia C. Atella , Eliane Fialho , Márcia C. Paes , Russolina B. Zingali , Jorge H. Petretski ^¶ , Elias W. Alves and Hatisaburo Masuda

From the  Departamento de Bioquímica Médica, Instituto de Ciências Biomédicas, Universidade Federal do Rio de Janeiro, P. O. Box 68041, Rio de Janeiro CEP 21941-590, RJ, Brasil, the ^¶ Escola Técnica Federal de Química do Rio de Janeiro, Rio de Janeiro 20010-000, RJ, Brasil, and the  Laboratório de Química e Função de Proteínas e Peptídeos, Centro de Biociências e Biotecnologia, Universidade Estadual do Norte Fluminense, Campos 28015-620, RJ, Brasil

A novel calcium-binding phosphoprotein was isolated from the oocytes of the blood-sucking bug Rhodnius prolixus. This protein exhibits an apparent molecular mass of 18 kDa on gel filtration, but migrates as an 8-kDa band on N-[2-hydroxy-1,1-bis(hydroxymethyl)ethyl]glycine/SDS-polyacrylamide gels. It has a high content of serine (24% of the total number of residues), and phosphoserine is the sole amino acid phosphorylated in vivo. A similar protein was partially purified from the hemolymph. It resembles the oocyte form of the protein in its NH₂-terminal sequence and its ability to be taken up by growing ovaries. ⁴⁵Ca binding to the oocyte phosphoprotein was determined after SDS-polyacrylamide gel electrophoresis followed by blotting on nitrocellulose membranes. Titration of Ca²⁺-binding sites shows a high capacity (50 mol/mol of protein), but a low affinity (K_0.5  10³ M). Based on these characteristics, we have named this protein Rhodnius calcium-binding phosphoprotein. It resembles phosvitin, a phosphoprotein present in the oocytes of nonmammalian vertebrates.

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